Nanoimaging for prion related diseases

Alexey V Krasnoslobodtsev, Alexander M. Portillo, Tanja Deckert-Gaudig, Volker Deckert, Yuri L Lyubchenko

Research output: Contribution to journalReview article

13 Citations (Scopus)

Abstract

Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading to the formation of aggregates and ultimately to neurodegeneration. Prion phenomenon is not restricted to humans. There are a number of prion-related diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle. All known prion diseases, collectively called transmissible spongiform encephalopathies (TSEs), are untreatable and fatal. Prion proteins were also found in some fungi where they are responsible for heritable traits. Prion proteins in fungi are easily accessible and provide a powerful model for understanding the general principles of prion phenomenon and molecular mechanisms of mammalian prion diseases. Presently, several fundamental questions related to prions remain unanswered. For example, it is not clear how prions cause the disease. Other unknowns include the nature and structure of infectious agent and how prions replicate. Generally, the phenomenon of misfolding of the prion protein into infectious conformations that have the ability to propagate their properties via aggregation is of significant interest. Despite the crucial importance of misfolding and aggregation, very little is currently known about the molecular mechanisms of these processes. While there is an apparent critical need to study molecular mechanisms underlying misfolding and aggregation, the detailed characterization of these single molecule processes is hindered by the limitation of conventional methods. Although some issues remain unresolved, much progress has been recently made primarily due to the application of nanoimaging tools. The use of nanoimaging methods shows great promise for understanding the molecular mechanisms of prion phenomenon, possibly leading toward early diagnosis and effective treatment of these devastating diseases. This review article summarizes recent reports which advanced our understanding of the prion phenomenon through the use of nanoimaging methods.

Original languageEnglish (US)
Pages (from-to)265-274
Number of pages10
JournalPrion
Volume4
Issue number4
DOIs
StatePublished - Oct 1 2010

Fingerprint

Prion Diseases
Prions
Bovine Spongiform Encephalopathy
Agglomeration
Fatal Familial Insomnia
Fungi
Gerstmann-Straussler-Scheinker Disease
Kuru
Creutzfeldt-Jakob Syndrome
Aptitude
Neurodegenerative Diseases
Early Diagnosis
Mammals
Proteins
Prion Proteins
Conformations

Keywords

  • Atomic force microscopy
  • Force spectroscopy
  • Nanomedicine
  • Prion
  • Protein misfolding

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience
  • Cell Biology
  • Infectious Diseases

Cite this

Nanoimaging for prion related diseases. / Krasnoslobodtsev, Alexey V; Portillo, Alexander M.; Deckert-Gaudig, Tanja; Deckert, Volker; Lyubchenko, Yuri L.

In: Prion, Vol. 4, No. 4, 01.10.2010, p. 265-274.

Research output: Contribution to journalReview article

Krasnoslobodtsev, AV, Portillo, AM, Deckert-Gaudig, T, Deckert, V & Lyubchenko, YL 2010, 'Nanoimaging for prion related diseases', Prion, vol. 4, no. 4, pp. 265-274. https://doi.org/10.4161/pri.4.4.13125
Krasnoslobodtsev, Alexey V ; Portillo, Alexander M. ; Deckert-Gaudig, Tanja ; Deckert, Volker ; Lyubchenko, Yuri L. / Nanoimaging for prion related diseases. In: Prion. 2010 ; Vol. 4, No. 4. pp. 265-274.
@article{4b6c23a31df5485dbe98cd715373d3e9,
title = "Nanoimaging for prion related diseases",
abstract = "Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading to the formation of aggregates and ultimately to neurodegeneration. Prion phenomenon is not restricted to humans. There are a number of prion-related diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as {"}mad cow disease{"}) in cattle. All known prion diseases, collectively called transmissible spongiform encephalopathies (TSEs), are untreatable and fatal. Prion proteins were also found in some fungi where they are responsible for heritable traits. Prion proteins in fungi are easily accessible and provide a powerful model for understanding the general principles of prion phenomenon and molecular mechanisms of mammalian prion diseases. Presently, several fundamental questions related to prions remain unanswered. For example, it is not clear how prions cause the disease. Other unknowns include the nature and structure of infectious agent and how prions replicate. Generally, the phenomenon of misfolding of the prion protein into infectious conformations that have the ability to propagate their properties via aggregation is of significant interest. Despite the crucial importance of misfolding and aggregation, very little is currently known about the molecular mechanisms of these processes. While there is an apparent critical need to study molecular mechanisms underlying misfolding and aggregation, the detailed characterization of these single molecule processes is hindered by the limitation of conventional methods. Although some issues remain unresolved, much progress has been recently made primarily due to the application of nanoimaging tools. The use of nanoimaging methods shows great promise for understanding the molecular mechanisms of prion phenomenon, possibly leading toward early diagnosis and effective treatment of these devastating diseases. This review article summarizes recent reports which advanced our understanding of the prion phenomenon through the use of nanoimaging methods.",
keywords = "Atomic force microscopy, Force spectroscopy, Nanomedicine, Prion, Protein misfolding",
author = "Krasnoslobodtsev, {Alexey V} and Portillo, {Alexander M.} and Tanja Deckert-Gaudig and Volker Deckert and Lyubchenko, {Yuri L}",
year = "2010",
month = "10",
day = "1",
doi = "10.4161/pri.4.4.13125",
language = "English (US)",
volume = "4",
pages = "265--274",
journal = "Prion",
issn = "1933-6896",
publisher = "Landes Bioscience",
number = "4",

}

TY - JOUR

T1 - Nanoimaging for prion related diseases

AU - Krasnoslobodtsev, Alexey V

AU - Portillo, Alexander M.

AU - Deckert-Gaudig, Tanja

AU - Deckert, Volker

AU - Lyubchenko, Yuri L

PY - 2010/10/1

Y1 - 2010/10/1

N2 - Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading to the formation of aggregates and ultimately to neurodegeneration. Prion phenomenon is not restricted to humans. There are a number of prion-related diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle. All known prion diseases, collectively called transmissible spongiform encephalopathies (TSEs), are untreatable and fatal. Prion proteins were also found in some fungi where they are responsible for heritable traits. Prion proteins in fungi are easily accessible and provide a powerful model for understanding the general principles of prion phenomenon and molecular mechanisms of mammalian prion diseases. Presently, several fundamental questions related to prions remain unanswered. For example, it is not clear how prions cause the disease. Other unknowns include the nature and structure of infectious agent and how prions replicate. Generally, the phenomenon of misfolding of the prion protein into infectious conformations that have the ability to propagate their properties via aggregation is of significant interest. Despite the crucial importance of misfolding and aggregation, very little is currently known about the molecular mechanisms of these processes. While there is an apparent critical need to study molecular mechanisms underlying misfolding and aggregation, the detailed characterization of these single molecule processes is hindered by the limitation of conventional methods. Although some issues remain unresolved, much progress has been recently made primarily due to the application of nanoimaging tools. The use of nanoimaging methods shows great promise for understanding the molecular mechanisms of prion phenomenon, possibly leading toward early diagnosis and effective treatment of these devastating diseases. This review article summarizes recent reports which advanced our understanding of the prion phenomenon through the use of nanoimaging methods.

AB - Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading to the formation of aggregates and ultimately to neurodegeneration. Prion phenomenon is not restricted to humans. There are a number of prion-related diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle. All known prion diseases, collectively called transmissible spongiform encephalopathies (TSEs), are untreatable and fatal. Prion proteins were also found in some fungi where they are responsible for heritable traits. Prion proteins in fungi are easily accessible and provide a powerful model for understanding the general principles of prion phenomenon and molecular mechanisms of mammalian prion diseases. Presently, several fundamental questions related to prions remain unanswered. For example, it is not clear how prions cause the disease. Other unknowns include the nature and structure of infectious agent and how prions replicate. Generally, the phenomenon of misfolding of the prion protein into infectious conformations that have the ability to propagate their properties via aggregation is of significant interest. Despite the crucial importance of misfolding and aggregation, very little is currently known about the molecular mechanisms of these processes. While there is an apparent critical need to study molecular mechanisms underlying misfolding and aggregation, the detailed characterization of these single molecule processes is hindered by the limitation of conventional methods. Although some issues remain unresolved, much progress has been recently made primarily due to the application of nanoimaging tools. The use of nanoimaging methods shows great promise for understanding the molecular mechanisms of prion phenomenon, possibly leading toward early diagnosis and effective treatment of these devastating diseases. This review article summarizes recent reports which advanced our understanding of the prion phenomenon through the use of nanoimaging methods.

KW - Atomic force microscopy

KW - Force spectroscopy

KW - Nanomedicine

KW - Prion

KW - Protein misfolding

UR - http://www.scopus.com/inward/record.url?scp=78650206856&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78650206856&partnerID=8YFLogxK

U2 - 10.4161/pri.4.4.13125

DO - 10.4161/pri.4.4.13125

M3 - Review article

VL - 4

SP - 265

EP - 274

JO - Prion

JF - Prion

SN - 1933-6896

IS - 4

ER -